ID   CUTI3_ASPFC             Reviewed;         217 AA.
AC   B0YEP5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable cutinase 3;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108};
DE   AltName: Full=Cutin hydrolase 3;
DE   Flags: Precursor;
GN   ORFNames=AFUB_099910;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (By similarity). Degrades cutin, a
CC       macromolecule that forms the structure of the plant cuticle (By
CC       similarity). {ECO:0000250|UniProtKB:P00590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10108};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; DS499603; EDP47389.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YEP5; -.
DR   SMR; B0YEP5; -.
DR   ESTHER; aspfu-q4w9z4; Cutinase.
DR   EnsemblFungi; EDP47389; EDP47389; AFUB_099910.
DR   VEuPathDB; FungiDB:AFUB_099910; -.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   PhylomeDB; B0YEP5; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   InterPro; IPR043580; CUTINASE_1.
DR   InterPro; IPR011150; Cutinase_monf.
DR   PANTHER; PTHR33630; PTHR33630; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   PRINTS; PR00129; CUTINASE.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00155; CUTINASE_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..217
FT                   /note="Probable cutinase 3"
FT                   /id="PRO_0000395253"
FT   ACT_SITE        129
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   SITE            50
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            130
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        39..118
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        65..79
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        180..187
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   217 AA;  22483 MW;  10735C585B7690FA CRC64;
     MSLRSLFVAG LATLALAVPA PQIQARQGMS SNELESGPCR DVTFIFARGS TEQGNMGLIV
     GPGVCSSLKK DLGSDKVACQ GVGGAYTAQL APNFLSQNTN QASINAATDM FDLANTKCPN
     TKIVAGGYSQ GSAVIDNTIQ ALGSDLKAKV KGVVLFGFTR NVADKGQIPG YPKDQTKIYC
     AVGDMVCVNT LIITPAHLTY GADAGDAAKF LASKVQE